FAA4 long-chain fatty acid-CoA ligase FAA4 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: FAA4
Official Full Name: long-chain fatty acid-CoA ligase FAA4
Primary source: SGD:S000004860
Locus tag: YMR246W
See related: AllianceGenome:SGD:S000004860; FungiDB:YMR246W; VEuPathDB:YMR246W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables long-chain fatty acid-CoA ligase activity. Involved in long-chain fatty acid import into cell; long-chain fatty-acyl-CoA metabolic process; and sphingoid long-chain base transport. Located in lipid droplet and plasma membrane. Used to study Sjogren-Larsson syndrome. Human ortholog(s) of this gene implicated in asthma; breast cancer; intellectual disability; non-syndromic X-linked intellectual disability 63; and prostate cancer. Orthologous to several human genes including ACSL4 (acyl-CoA synthetase long chain family member 4). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See FAA4 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (759807..761891)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Quantitative live-cell PALM reveals nanoscopic Faa4 redistributions and dynamics on lipid droplets during metabolic transitions of yeast.
Title: Quantitative live-cell PALM reveals nanoscopic Faa4 redistributions and dynamics on lipid droplets during metabolic transitions of yeast.
here we revealed that ACSs (Faa1 and Faa4 in yeast and ACSL1, ACSL4, ACSL5, ACSL6, and ACSVL4 in mammals) are involved in LCB uptake. In addition, we provided important insight into the molecular mechanism of LCFA transport
Title: Long-chain bases of sphingolipids are transported into cells via the acyl-CoA synthetases.
recycling of endogenous fatty acids generated in the course of lipid remodelling is a major task of both acyl-CoA synthetases Faa1p and Faa4p
Title: Mutants of Saccharomyces cerevisiae deficient in acyl-CoA synthetases secrete fatty acids due to interrupted fatty acid recycling.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ligase activity	IEA Inferred from Electronic Annotation more info
enables long-chain fatty acid-CoA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables long-chain fatty acid-CoA ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables long-chain fatty acid-CoA ligase activity	IEA Inferred from Electronic Annotation more info
enables long-chain fatty acid-CoA ligase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables long-chain fatty acid-CoA ligase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in fatty acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in long-chain fatty acid import into cell	IGI Inferred from Genetic Interaction more info	PubMed
involved_in long-chain fatty acid metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in long-chain fatty-acyl-CoA metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in long-chain fatty-acyl-CoA metabolic process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in long-chain fatty-acyl-CoA metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in sphingoid long-chain base transport	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasmic stress granule	HDA more info	PubMed
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
is_active_in lipid droplet	IBA Inferred from Biological aspect of Ancestor more info
located_in lipid droplet	IDA Inferred from Direct Assay more info	PubMed
located_in lipid droplet	IEA Inferred from Electronic Annotation more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: long-chain fatty acid-CoA ligase FAA4

NP_013974.1

EC 6.2.1.3

Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; role in stationary phase survival; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms cytoplasmic foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

759807..761891

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182754.1 → NP_013974.1 TPA: long-chain fatty acid-CoA ligase FAA4 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013974.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W073, P47912, Q05743

UniProtKB/TrEMBL

A6ZMW0

Conserved Domains (2) summary

PRK04319
Location:230 → 285

PRK04319; acetyl-CoA synthetase; Provisional

cd17639
Location:96 → 678

LC_FACS_euk1; Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins